Literature DB >> 21139219

Cloning, expression, purification, crystallization and preliminary X-ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosis.

Dhabaleswar Patra1, R Srikalaivani, Ashish Misra, D D Singh, M Selvaraj, M Vijayan.   

Abstract

A secreted lectin, Rv1419, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized and the crystals have been characterized. This represents the first X-ray investigation of a lectin or lectin-like molecule from the pathogen. The cubic crystals contain one molecule in the asymmetric unit. Sequence comparisons indicate that the lectin has a β-trefoil fold and belongs to a well characterized family of carbohydrate-binding modules. Structural analysis of the crystals is in progress.

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Year:  2010        PMID： 21139219      PMCID： PMC2998378          DOI： 10.1107/S1744309110042892

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  40 in total

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6.  Solvent content of protein crystals.

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9.  The 1.25 A resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site.

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  3 in total

1.  Cloning, expression, purification, crystallization and preliminary X-ray studies of the mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis.

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Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-04-28

Review 2.  Mycobacterial Adhesion: From Hydrophobic to Receptor-Ligand Interactions.

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Review 3.  Lectins of Mycobacterium tuberculosis - rarely studied proteins.

Authors:  Katharina Kolbe; Sri Kumar Veleti; Norbert Reiling; Thisbe K Lindhorst
Journal:  Beilstein J Org Chem       Date:  2019-01-02       Impact factor: 2.883
  3 in total

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